Bacillus thuringiensis (Bt) produces inclusions that are composed of proteins known as crystal proteins or Cry toxins. Due to their high specificity and their safety to humans and the environment, these Cry toxins are considered to be valuable alternatives to chemical pesticides in insect control programs. It is believed that Cry toxin-induced membrane pore formation is responsible for insect toxicity. The molecular mechanism of pore formation involves recognition and subsequent binding of the toxin to membrane receptors. This binding is accompanied by toxin oligomerization and transfer of domain I helices of the toxin to the lipid-water interface. This toxin insertion creates pores that lyse the cells. Several receptors from lepidopteran, coleopteran, and dipteran insects have been well characterized. This paper provides an overview of the understanding of the interactions between Cry toxin and multiple receptors in mosquitoes, in particular Aedes aegypti and reviews the manner by which the receptors were identified and characterized, with a focus on three proteins, cadherin, alkaline phosphatase, and aminopeptidase-N.